ID NAB2_YEAST Reviewed; 525 AA. AC P32505; D6VU26; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 27-MAR-2024, entry version 192. DE RecName: Full=Nuclear polyadenylated RNA-binding protein NAB2 {ECO:0000303|PubMed:8474438}; GN Name=NAB2 {ECO:0000303|PubMed:8474438}; OrderedLocusNames=YGL122C; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION. RC STRAIN=ATCC 208279 / BJ926; RX PubMed=8474438; DOI=10.1128/mcb.13.5.2730-2741.1993; RA Anderson J.T., Wilson S.M., Datar K.V., Swanson M.S.; RT "NAB2: a yeast nuclear polyadenylated RNA-binding protein essential for RT cell viability."; RL Mol. Cell. Biol. 13:2730-2741(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169869; RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H., RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."; RL Nature 387:81-84(1997). RN [3] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [5] RP FUNCTION. RX PubMed=11927564; DOI=10.1093/emboj/21.7.1800; RA Hector R.E., Nykamp K.R., Dheur S., Anderson J.T., Non P.J., Urbinati C.R., RA Wilson S.M., Minvielle-Sebastia L., Swanson M.S.; RT "Dual requirement for yeast hnRNP Nab2p in mRNA poly(A) tail length control RT and nuclear export."; RL EMBO J. 21:1800-1810(2002). RN [6] RP FUNCTION, SUBCELLULAR LOCATION, AND METHYLATION BY HMT1. RX PubMed=11779864; DOI=10.1074/jbc.m110053200; RA Green D.M., Marfatia K.A., Crafton E.B., Zhang X., Cheng X., Corbett A.H.; RT "Nab2p is required for poly(A) RNA export in Saccharomyces cerevisiae and RT is regulated by arginine methylation via Hmt1p."; RL J. Biol. Chem. 277:7752-7760(2002). RN [7] RP DOMAIN. RX PubMed=12496292; DOI=10.1074/jbc.m207571200; RA Marfatia K.A., Crafton E.B., Green D.M., Corbett A.H.; RT "Domain analysis of the Saccharomyces cerevisiae heterogeneous nuclear RT ribonucleoprotein, Nab2p. Dissecting the requirements for Nab2p-facilitated RT poly(A) RNA export."; RL J. Biol. Chem. 278:6731-6740(2003). RN [8] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [9] RP INTERACTION WITH MLP1. RX PubMed=18682389; DOI=10.1074/jbc.m803649200; RA Fasken M.B., Stewart M., Corbett A.H.; RT "Functional significance of the interaction between the mRNA-binding RT protein, Nab2, and the nuclear pore-associated protein, Mlp1, in mRNA RT export."; RL J. Biol. Chem. 283:27130-27143(2008). RN [10] RP FUNCTION. RX PubMed=19840948; DOI=10.1074/jbc.m109.062034; RA Batisse J., Batisse C., Budd A., Boettcher B., Hurt E.; RT "Purification of nuclear poly(A)-binding protein Nab2 reveals association RT with the yeast transcriptome and a messenger ribonucleoprotein core RT structure."; RL J. Biol. Chem. 284:34911-34917(2009). RN [11] RP SUBCELLULAR LOCATION. RX PubMed=23222640; DOI=10.1038/nsmb.2468; RA Mitchell S.F., Jain S., She M., Parker R.; RT "Global analysis of yeast mRNPs."; RL Nat. Struct. Mol. Biol. 20:127-133(2013). RN [12] RP METHYLATION AT ARG-222. RX PubMed=26046779; DOI=10.1002/pmic.201500032; RA Plank M., Fischer R., Geoghegan V., Charles P.D., Konietzny R., Acuto O., RA Pears C., Schofield C.J., Kessler B.M.; RT "Expanding the yeast protein arginine methylome."; RL Proteomics 15:3232-3243(2015). RN [13] RP METHYLATION AT ARG-209, AND PHOSPHORYLATION AT THR-254. RX PubMed=33856219; DOI=10.1021/acs.jproteome.0c00927; RA Hamey J.J., Nguyen A., Wilkins M.R.; RT "Discovery of arginine methylation, phosphorylation, and their co- RT occurrence in condensate-associated proteins in Saccharomyces cerevisiae."; RL J. Proteome Res. 20:2420-2434(2021). RN [14] {ECO:0007744|PDB:2JPS, ECO:0007744|PDB:2V75} RP STRUCTURE BY NMR OF 1-105, AND INTERACTION WITH MLP1. RX PubMed=18190927; DOI=10.1016/j.jmb.2007.11.087; RA Grant R.P., Marshall N.J., Yang J.C., Fasken M.B., Kelly S.M., RA Harreman M.T., Neuhaus D., Corbett A.H., Stewart M.; RT "Structure of the N-terminal Mlp1-binding domain of the Saccharomyces RT cerevisiae mRNA-binding protein, Nab2."; RL J. Mol. Biol. 376:1048-1059(2008). RN [15] {ECO:0007744|PDB:3LCN} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-105 IN COMPLEX WITH ZINC. RX PubMed=20463024; DOI=10.1074/jbc.m110.107276; RA Zheng C., Fasken M.B., Marshall N.J., Brockmann C., Rubinson M.E., RA Wente S.R., Corbett A.H., Stewart M.; RT "Structural basis for the function of the Saccharomyces cerevisiae Gfd1 RT protein in mRNA nuclear export."; RL J. Biol. Chem. 285:20704-20715(2010). RN [16] {ECO:0007744|PDB:2LHN} RP STRUCTURE BY NMR OF 409-483, AND FUNCTION. RX PubMed=22560733; DOI=10.1016/j.str.2012.03.011; RA Brockmann C., Soucek S., Kuhlmann S.I., Mills-Lujan K., Kelly S.M., RA Yang J.C., Iglesias N., Stutz F., Corbett A.H., Neuhaus D., Stewart M.; RT "Structural basis for polyadenosine-RNA binding by Nab2 Zn fingers and its RT function in mRNA nuclear export."; RL Structure 20:1007-1018(2012). RN [17] {ECO:0007744|PDB:4JLQ} RP X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 205-242. RX PubMed=23535894; DOI=10.1007/s10969-013-9150-1; RA Soniat M., Sampathkumar P., Collett G., Gizzi A.S., Banu R.N., Bhosle R.C., RA Chamala S., Chowdhury S., Fiser A., Glenn A.S., Hammonds J., Hillerich B., RA Khafizov K., Love J.D., Matikainen B., Seidel R.D., Toro R., RA Rajesh Kumar P., Bonanno J.B., Chook Y.M., Almo S.C.; RT "Crystal structure of human Karyopherin beta2 bound to the PY-NLS of RT Saccharomyces cerevisiae Nab2."; RL J. Struct. Funct. Genomics 14:31-35(2013). RN [18] {ECO:0007744|PDB:3ZJ1, ECO:0007744|PDB:3ZJ2} RP STRUCTURE BY NMR OF 253-333. RX PubMed=23994011; DOI=10.1016/j.str.2013.07.019; RA Martinez-Lumbreras S., Santiveri C.M., Mirassou Y., Zorrilla S., RA Perez-Canadillas J.M.; RT "Two singular types of CCCH tandem zinc finger in Nab2p contribute to RT polyadenosine RNA recognition."; RL Structure 21:1800-1811(2013). RN [19] {ECO:0007744|PDB:5L2L} RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 407-483 IN COMPLEX WITH ZINC, AND RP DOMAIN. RX PubMed=28180315; DOI=10.1093/nar/gkw1224; RA Aibara S., Gordon J.M., Riesterer A.S., McLaughlin S.H., Stewart M.; RT "Structural basis for the dimerization of Nab2 generated by RNA binding RT provides insight into its contribution to both poly(A) tail length RT determination and transcript compaction in Saccharomyces cerevisiae."; RL Nucleic Acids Res. 45:1529-1538(2017). CC -!- FUNCTION: Essential protein that binds to polyadenylated RNA and CC single-stranded DNA (PubMed:8474438). It may be involved not only in CC RNA processing but also in transcription regulation. Associates CC directly with nascent RNA polymerase II transcripts and remain CC associated during subsequent nuclear RNA processing reactions CC (Probable). Involved in mRNA poly(A) tail length control and nuclear CC export (PubMed:11927564, PubMed:11779864). Functions in surveillance CC and the packaging leading to generation of export-competent mRNPs. CC Controls both mRNP compaction that facilitates movement through nuclear CC pore complexes and the length of transcript poly(A) tails CC (PubMed:19840948, PubMed:22560733). {ECO:0000269|PubMed:11779864, CC ECO:0000269|PubMed:11927564, ECO:0000269|PubMed:19840948, CC ECO:0000269|PubMed:22560733, ECO:0000269|PubMed:8474438, CC ECO:0000305|PubMed:8474438}. CC -!- SUBUNIT: Interacts with MLP1. {ECO:0000269|PubMed:18190927, CC ECO:0000269|PubMed:18682389}. CC -!- INTERACTION: CC P32505; Q04839: GFD1; NbExp=7; IntAct=EBI-11770, EBI-27549; CC P32505; P38074: HMT1; NbExp=2; IntAct=EBI-11770, EBI-8394; CC P32505; P38217: KAP104; NbExp=4; IntAct=EBI-11770, EBI-9152; CC P32505; Q02455: MLP1; NbExp=4; IntAct=EBI-11770, EBI-11009; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11779864, CC ECO:0000269|PubMed:23222640, ECO:0000269|PubMed:8474438}. Cytoplasm CC {ECO:0000269|PubMed:11779864}. Note=Localizes to the nucleus at steady- CC state, it shuttles between nucleus and cytoplasm. CC {ECO:0000269|PubMed:11779864}. CC -!- DOMAIN: The N-terminal domain is required for nuclear export of both CC poly(A) RNA and NAB2. {ECO:0000269|PubMed:12496292}. CC -!- DOMAIN: The RGG domain is important for NAB2 import. CC {ECO:0000269|PubMed:12496292}. CC -!- DOMAIN: Contains seven CCCH Zn fingers that bind to A-rich RNAs and CC fingers 5 to 7 are critical for these function (PubMed:12496292, CC PubMed:22560733, PubMed:28180315). Binding A(11)G RNA induces CC dimerization of Zn fingers 5-7 mediated by the spatial arrangement of CC the fingers promoting each RNA chain binding two protein chains CC (PubMed:28180315). {ECO:0000269|PubMed:12496292, CC ECO:0000269|PubMed:22560733, ECO:0000269|PubMed:28180315}. CC -!- PTM: Methylated by HMT1. {ECO:0000269|PubMed:11779864}. CC -!- MISCELLANEOUS: Present with 9670 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the NAB2 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L10288; AAA34819.1; -; Genomic_DNA. DR EMBL; L08079; AAA34820.1; -; Genomic_DNA. DR EMBL; Z72644; CAA96830.1; -; Genomic_DNA. DR EMBL; AY723810; AAU09727.1; -; Genomic_DNA. DR EMBL; BK006941; DAA07987.1; -; Genomic_DNA. DR PIR; B48058; B48058. DR RefSeq; NP_011393.3; NM_001180987.3. DR PDB; 2JPS; NMR; -; A=1-105. DR PDB; 2LHN; NMR; -; A=409-483. DR PDB; 2V75; X-ray; 1.80 A; A=1-104. DR PDB; 3LCN; X-ray; 2.00 A; A/B=1-105. DR PDB; 3ZJ1; NMR; -; A=253-333. DR PDB; 3ZJ2; NMR; -; A=333-401. DR PDB; 4JLQ; X-ray; 3.04 A; B=205-242. DR PDB; 5L2L; X-ray; 1.55 A; A/B/E/F=409-483. DR PDBsum; 2JPS; -. DR PDBsum; 2LHN; -. DR PDBsum; 2V75; -. DR PDBsum; 3LCN; -. DR PDBsum; 3ZJ1; -. DR PDBsum; 3ZJ2; -. DR PDBsum; 4JLQ; -. DR PDBsum; 5L2L; -. DR AlphaFoldDB; P32505; -. DR BMRB; P32505; -. DR SMR; P32505; -. DR BioGRID; 33129; 2772. DR DIP; DIP-1331N; -. DR IntAct; P32505; 16. DR MINT; P32505; -. DR STRING; 4932.YGL122C; -. DR iPTMnet; P32505; -. DR MaxQB; P32505; -. DR PaxDb; 4932-YGL122C; -. DR PeptideAtlas; P32505; -. DR EnsemblFungi; YGL122C_mRNA; YGL122C; YGL122C. DR GeneID; 852755; -. DR KEGG; sce:YGL122C; -. DR AGR; SGD:S000003090; -. DR SGD; S000003090; NAB2. DR VEuPathDB; FungiDB:YGL122C; -. DR eggNOG; KOG3702; Eukaryota. DR GeneTree; ENSGT00440000038430; -. DR HOGENOM; CLU_037973_1_0_1; -. DR InParanoid; P32505; -. DR OMA; VAEYIVL; -. DR OrthoDB; 1369725at2759; -. DR BioCyc; YEAST:G3O-30619-MONOMER; -. DR BioGRID-ORCS; 852755; 7 hits in 10 CRISPR screens. DR EvolutionaryTrace; P32505; -. DR PRO; PR:P32505; -. DR Proteomes; UP000002311; Chromosome VII. DR RNAct; P32505; Protein. DR GO; GO:0005737; C:cytoplasm; IDA:SGD. DR GO; GO:0005634; C:nucleus; IDA:SGD. DR GO; GO:0008097; F:5S rRNA binding; IDA:SGD. DR GO; GO:0008312; F:7S RNA binding; IDA:SGD. DR GO; GO:0003729; F:mRNA binding; HDA:SGD. DR GO; GO:0008143; F:poly(A) binding; IDA:SGD. DR GO; GO:0033204; F:ribonuclease P RNA binding; IDA:SGD. DR GO; GO:0000049; F:tRNA binding; IDA:SGD. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:1900364; P:negative regulation of mRNA polyadenylation; IBA:GO_Central. DR GO; GO:1900152; P:negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IGI:SGD. DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:SGD. DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; IDA:SGD. DR GO; GO:0043488; P:regulation of mRNA stability; IMP:SGD. DR Gene3D; 4.10.1000.40; -; 3. DR Gene3D; 1.10.340.40; Nuclear abundant poly(A) RNA-bind protein 2, N-terminal domain; 1. DR IDEAL; IID50171; -. DR InterPro; IPR040366; Nab2/ZC3H14. DR InterPro; IPR043094; Nab2/ZC3H14_N_sf. DR InterPro; IPR021083; Nab2_N. DR InterPro; IPR049017; Nab2_Znf4. DR InterPro; IPR041044; Nab2p_Zf1. DR InterPro; IPR048410; Znf-CCCH_2-like_3. DR PANTHER; PTHR14738; ZINC FINGER CCCH DOMAIN-CONTAINING PROTEIN 14; 1. DR PANTHER; PTHR14738:SF29; ZINC FINGER CCCH DOMAIN-CONTAINING PROTEIN 14; 1. DR Pfam; PF11517; Nab2; 1. DR Pfam; PF21803; Nab2-zf4; 1. DR Pfam; PF18260; Nab2p_Zf1; 1. DR Pfam; PF14608; zf-CCCH_2; 4. DR Pfam; PF21457; zf-CCCH_2-like_3; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Metal-binding; Methylation; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger. FT CHAIN 1..525 FT /note="Nuclear polyadenylated RNA-binding protein NAB2" FT /id="PRO_0000096687" FT REPEAT 121..124 FT /note="1" FT /evidence="ECO:0000305" FT REPEAT 125..128 FT /note="2" FT /evidence="ECO:0000305" FT REPEAT 129..132 FT /note="3" FT /evidence="ECO:0000305" FT REPEAT 133..136 FT /note="4" FT /evidence="ECO:0000305" FT REPEAT 137..140 FT /note="5" FT /evidence="ECO:0000305" FT REPEAT 141..144 FT /note="6" FT /evidence="ECO:0000305" FT REPEAT 145..148 FT /note="7" FT /evidence="ECO:0000305" FT REPEAT 149..152 FT /note="8" FT /evidence="ECO:0000305" FT REPEAT 153..156 FT /note="9" FT /evidence="ECO:0000305" FT REPEAT 157..160 FT /note="10; approximate" FT /evidence="ECO:0000305" FT ZN_FING 262..278 FT /note="C3H1-type 1" FT /evidence="ECO:0000255, ECO:0000305|PubMed:23994011" FT ZN_FING 283..300 FT /note="C3H1-type 2" FT /evidence="ECO:0000255, ECO:0000305|PubMed:23994011" FT ZN_FING 340..355 FT /note="C3H1-type 3" FT /evidence="ECO:0000255, ECO:0000305|PubMed:23994011" FT ZN_FING 371..386 FT /note="C3H1-type 4" FT /evidence="ECO:0000255, ECO:0000305|PubMed:23994011" FT ZN_FING 415..430 FT /note="C3H1-type 5" FT /evidence="ECO:0000255, ECO:0000305|PubMed:22560733" FT ZN_FING 437..452 FT /note="C3H1-type 6" FT /evidence="ECO:0000255, ECO:0000305|PubMed:22560733" FT ZN_FING 458..473 FT /note="C3H1-type 7" FT /evidence="ECO:0000255, ECO:0000305|PubMed:22560733" FT REGION 102..160 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 121..156 FT /note="10 X 4 AA tandem repeats of Q-Q-Q-P" FT /evidence="ECO:0000305" FT REGION 196..236 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 209..239 FT /note="PY-NLS nuclear localization signal" FT /evidence="ECO:0000305|PubMed:23535894" FT REGION 209..228 FT /note="RNA-binding RGG-box" FT /evidence="ECO:0000250" FT REGION 503..525 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 507..525 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 209 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000269|PubMed:33856219" FT MOD_RES 222 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000269|PubMed:26046779" FT MOD_RES 254 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:33856219" FT VARIANT 130..157 FT /note="Missing (in YJA512)" FT HELIX 7..18 FT /evidence="ECO:0007829|PDB:2V75" FT HELIX 28..40 FT /evidence="ECO:0007829|PDB:2V75" FT HELIX 45..55 FT /evidence="ECO:0007829|PDB:2V75" FT HELIX 61..79 FT /evidence="ECO:0007829|PDB:2V75" FT HELIX 84..93 FT /evidence="ECO:0007829|PDB:2V75" FT TURN 269..273 FT /evidence="ECO:0007829|PDB:3ZJ1" FT TURN 293..295 FT /evidence="ECO:0007829|PDB:3ZJ1" FT STRAND 297..299 FT /evidence="ECO:0007829|PDB:3ZJ1" FT STRAND 301..303 FT /evidence="ECO:0007829|PDB:3ZJ1" FT HELIX 305..326 FT /evidence="ECO:0007829|PDB:3ZJ1" FT STRAND 328..330 FT /evidence="ECO:0007829|PDB:3ZJ1" FT HELIX 343..345 FT /evidence="ECO:0007829|PDB:3ZJ2" FT STRAND 353..355 FT /evidence="ECO:0007829|PDB:3ZJ2" FT HELIX 374..376 FT /evidence="ECO:0007829|PDB:3ZJ2" FT STRAND 384..387 FT /evidence="ECO:0007829|PDB:3ZJ2" FT HELIX 390..393 FT /evidence="ECO:0007829|PDB:3ZJ2" FT STRAND 412..414 FT /evidence="ECO:0007829|PDB:5L2L" FT HELIX 418..420 FT /evidence="ECO:0007829|PDB:5L2L" FT STRAND 427..429 FT /evidence="ECO:0007829|PDB:2LHN" FT STRAND 433..436 FT /evidence="ECO:0007829|PDB:5L2L" FT HELIX 440..442 FT /evidence="ECO:0007829|PDB:5L2L" FT STRAND 455..457 FT /evidence="ECO:0007829|PDB:5L2L" FT HELIX 461..463 FT /evidence="ECO:0007829|PDB:5L2L" FT STRAND 470..472 FT /evidence="ECO:0007829|PDB:2LHN" SQ SEQUENCE 525 AA; 58321 MW; 40335C3D4658DD91 CRC64; MSQEQYTENL KVIVAEKLAG IPNFNEDIKY VAEYIVLLIV NGGTVESVVD ELASLFDSVS RDTLANVVQT AFFALEALQQ GESAENIVSK IRMMNAQSLG QSDIAQQQQQ QQQQQQPDIA QQQPQQQPQQ QPQQQPQQQP QQQPQQQPQQ QPQQQPQLQP LQPQLGTQNA MQTDAPATPS PISAFSGVVN AAAPPQFAPV DNSQRFTQRG GGAVGKNRRG GRGGNRGGRN NNSTRFNPLA KALGMAGESN MNFTPTKKEG RCRLFPHCPL GRSCPHAHPT KVCNEYPNCP KPPGTCEFLH PNEDEELMKE MERTREEFQK RKADLLAAKR KPVQTGIVLC KFGALCSNPS CPFGHPTPAN EDAKVIDLMW CDKNLTCDNP ECRKAHSSLS KIKEVKPISQ KKAAPPPVEK SLEQCKFGTH CTNKRCKYRH ARSHIMCREG ANCTRIDCLF GHPINEDCRF GVNCKNIYCL FRHPPGRVLP EKKGAAPNSN VPTNERPFAL PENAIIENAP PQTSFTHQEQ DTEMN //